AC   MF_03009;
DC   Protein; auto
TR   HAMAP; MF_03009; -; 1; level=0
XX
Names: eIF3j
XX
ID   EIF3J
case <OC:Vertebrata>
DE   RecName: Full=Eukaryotic translation initiation factor 3 subunit J;
DE            Short=eIF3j;
DE   AltName: Full=Eukaryotic translation initiation factor 3 subunit 1;
DE   AltName: Full=eIF-3-alpha;
DE   AltName: Full=eIF3 p35;
else case <OC:Fungi>
DE   RecName: Full=Eukaryotic translation initiation factor 3 subunit J;
DE            Short=eIF3j;
DE   AltName: Full=Eukaryotic translation initiation factor 3 30 kDa subunit homolog;
DE            Short=eIF-3 30 kDa subunit homolog;
else
DE   RecName: Full=Eukaryotic translation initiation factor 3 subunit J;
DE            Short=eIF3j;
end case
case <OC:Vertebrata>
GN   Name=EIF3J; Synonyms=EIF3S1;
else case <OC:Drosophilidae>
GN   Name=eIF3j; Synonyms=Adam;
else case <OC:Fungi>
GN   Name=HCR1;
end case
XX
case <OC:Mammalia>
CC   -!- FUNCTION: Component of the eukaryotic translation initiation factor 3
CC       (eIF-3) complex, which is required for several steps in the initiation
CC       of protein synthesis. The eIF-3 complex associates with the 40S
CC       ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-
CC       2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex
CC       (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC
CC       and scanning of the mRNA for AUG recognition. The eIF-3 complex is also
CC       required for disassembly and recycling of post-termination ribosomal
CC       complexes and subsequently prevents premature joining of the 40S and
CC       60S ribosomal subunits prior to initiation. The eIF-3 complex
CC       specifically targets and initiates translation of a subset of mRNAs
CC       involved in cell proliferation, including cell cycling, differentiation
CC       and apoptosis, and uses different modes of RNA stem-loop binding to
CC       exert either translational activation or repression. This subunit binds
CC       directly within the mRNA entry channel of the 40S ribosome to the
CC       aminoacyl (A) site. It may regulate the interaction between the 43S PIC
CC       and mRNA.
else
CC   -!- FUNCTION: Component of the eukaryotic translation initiation factor 3
CC       (eIF-3) complex, which is involved in protein synthesis of a
CC       specialized repertoire of mRNAs and, together with other initiation
CC       factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S
CC       ribosome. The eIF-3 complex specifically targets and initiates
CC       translation of a subset of mRNAs involved in cell proliferation.
end case
case <OC:Mammalia>
CC   -!- SUBUNIT: Component of the eukaryotic translation initiation factor 3
CC       (eIF-3) complex, which is composed of 13 subunits: EIF3A, EIF3B, EIF3C,
CC       EIF3D, EIF3E, EIF3F, EIF3G, EIF3H, EIF3I, EIF3J, EIF3K, EIF3L and
CC       EIF3M. The eIF-3 complex appears to include 3 stable modules: module A
CC       is composed of EIF3A, EIF3B, EIF3G and EIF3I; module B is composed of
CC       EIF3F, EIF3H, and EIF3M; and module C is composed of EIF3C, EIF3D,
CC       EIF3E, EIF3K and EIF3L. EIF3C of module C binds EIF3B of module A and
CC       EIF3H of module B, thereby linking the three modules. EIF3J is a labile
CC       subunit that binds to the eIF-3 complex via EIF3B. The eIF-3 complex
CC       interacts with RPS6KB1 under conditions of nutrient depletion.
CC       Mitogenic stimulation leads to binding and activation of a complex
CC       composed of MTOR and RPTOR, leading to phosphorylation and release of
CC       RPS6KB1 and binding of EIF4B to eIF-3.
else case <OC:Vertebrata> and not <OC:Mammalia>
CC   -!- SUBUNIT: Component of the eukaryotic translation initiation factor 3
CC       (eIF-3) complex, which is composed of 13 subunits: @gn(EIF3A),
CC       @gn(EIF3B), @gn(EIF3C), @gn(EIF3D), @gn(EIF3E), @gn(EIF3F), @gn(EIF3G),
CC       @gn(EIF3H), @gn(EIF3I), @gn(EIF3J), @gn(EIF3K), @gn(EIF3L) and
CC       @gn(EIF3M).
else case <OC:Drosophilidae>
CC   -!- SUBUNIT: Component of the eukaryotic translation initiation factor 3
CC       (eIF-3) complex. The eIF-3 complex interacts with pix.
else
CC   -!- SUBUNIT: Component of the eukaryotic translation initiation factor 3
CC       (eIF-3) complex.
end case
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
case <OC:Mammalia>
CC   -!- PTM: Phosphorylated. Phosphorylation is enhanced upon serum
CC       stimulation.
end case
CC   -!- SIMILARITY: Belongs to the eIF-3 subunit J family.
XX
DR   Pfam; PF08597; eIF3_subunit; 1; trigger=no
DR   General; Coiled_coil; -; 0-unlimited; trigger=yes
XX
KW   Cytoplasm
KW   Initiation factor
KW   Protein biosynthesis
case <FTGroup:1>
KW   Acetylation
end case
case <OC:Mammalia>
KW   Phosphoprotein
end case
XX
GO   GO:0003743; F:translation initiation factor activity
GO   GO:0001732; P:formation of cytoplasmic translation initiation complex
GO   GO:0002183; P:cytoplasmic translational initiation
GO   GO:0005737; C:cytoplasm
GO   GO:0005852; C:eukaryotic translation initiation factor 3 complex
GO   GO:0016282; C:eukaryotic 43S preinitiation complex
GO   GO:0033290; C:eukaryotic 48S preinitiation complex
XX
FT   From: EIF3J_HUMAN (O75822)
case <OC:Mammalia>
FT   INIT_MET        Nter
FT                   /note="Removed"
FT   Group: 1; Condition: M
FT   REGION          1..69
FT                   /note="Sufficient for interaction with EIF3B"
FT   REGION          243..258
FT                   /note="Promotes stable association with the 40S ribosome"
FT   MOD_RES         Nter+1
FT                   /note="N-acetylalanine"
FT   Group: 1; Condition: A
FT   MOD_RES         11
FT                   /note="Phosphoserine"
FT   Condition: S
FT   MOD_RES         13
FT                   /note="Phosphoserine"
FT   Condition: S
FT   MOD_RES         20
FT                   /note="Phosphoserine"
FT   Condition: S
FT   MOD_RES         109
FT                   /note="Phosphothreonine"
FT   Condition: T
end case
XX
Size: 211-289;
Related: None;
Template: O75822; Q66JS6; Q05775;
Scope:
 Eukaryota
Fusion:
 Nter: None
 Cter: None
Duplicate: in DANRE
Plasmid: None
Comments: None
XX
# Revision 1.16 2021/08/12
//